Caching of a chameleon segment facilitates folding of a protein with end-to-end beta-sheet.
We report results from all-atom simulations of a 49-residue C-terminal fragment of TOP7 in implicit solvent. Using parallel tempering simulations with high statistics, we probe the thermodynamic properties of the protein over a large range of temperatures and evaluate its free energy landscape at room temperature. Our results confirm that the protein folds by a caching mechanism that relies on a chameleon segment. This mechanism differs from the one seen in high-temperature unfolding simulations. Finally, we discuss a possible mechanism for dimerization of the protein.
Mohanty
Sandipan
S
John von Neumann-Institut für Computing, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Hansmann
Ulrich H E
UH
D019281:Dimerization; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics